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http://prism.ccbb.ku.edu.tr/hotregion/index.php
Hot spots are energetically important residues at protein interfaces and they are not randomly distributed across the interface but rather clustered. These clustered hot spots form hot regions. Hot regions are important for the stability of protein complexes, as well as providing specificity to binding sites. HotRegion provides the hot region information of the interfaces by using predicted hot spot residues, and structural properties of these interface residues such as pair potentials of interface residues, accessible surface area (ASA) and relative ASA values of interface residues of both monomer and complex forms of proteins. Also, the 3D visualization of the interface and interactions among hot spot residues are provided. The number of interfaces in the database is 147909 and still growing.
Proper citation: HotRegion - A Database of Cooperative Hotspots (RRID:SCR_006022) Copy
DOMMINO is a comprehensive structural database on macromolecular interactions. As of June, 2011, it contains more than 407,000 binary interactions. The distinctive features of DOMMINO are: # Automated updates: DOMMINO is fully automated and is designed to update itself on a weekly basis, one day after a PDB weekly update. Thus, the community will be able to study macromolecular interactions almost immediately after they are released by PDB. # Coverage of non-domain mediated interactions: In addition to domain-domain and domain-peptide interactions the database characterizes the interaction between domains and unstructured protein regions that are not parts of a domain, such as inter-domain linkers and N- and C-termini. The interactions that involve the latter unstructured parts of proteins have been included to the database for the first time providing additional ~186,000 interactions (~45% of the total number of interactions, as of June, 2011). # Coverage of new structural domains: DOMMINO employs one of the most accurate structural classifications of proteins, SCOP. In addition to the existing SCOP-annotated domains, we employ a state-of-the-art machine learning approach to classify newer protein structures into existing SCOP families. With the progress of structural genomics, we do not expect a significant growth of the number of structurally novel folds or protein families and therefore our method allows covering almost all new protein structures. In total, using this predictive approach has allowed us to add more than 261,000 new interactions, almost twice as many as existing SCOP-annotated interactions. # The web-interface is designed to give the user a possibility of a flexible search as well as the capability to study macromolecular interactions in a PDB structure at the interaction network level and at the individual interface level. The web interface of the DOMMINO database includes a comprehensive list of help topics linked to the specific actions. In addition, we have designed a step-by-step tutorial that covers all aspects of working with the data from DOMMINO using the web interface.
Proper citation: DOMMINO - Database Of MacroMolecular INteractiOns (RRID:SCR_005958) Copy
http://www.jcvi.org/charprotdb/index.cgi/home
The Characterized Protein Database, CharProtDB, is designed and being developed as a resource of expertly curated, experimentally characterized proteins described in published literature. For each protein record in CharProtDB, storage of several data types is supported. It includes functional annotation (several instances of protein names and gene symbols) taxonomic classification, literature links, specific Gene Ontology (GO) terms and GO evidence codes, EC (Enzyme Commisssion) and TC (Transport Classification) numbers and protein sequence. Additionally, each protein record is associated with cross links to all public accessions in major protein databases as ��synonymous accessions��. Each of the above data types can be linked to as many literature references as possible. Every CharProtDB entry requires minimum data types to be furnished. They are protein name, GO terms and supporting reference(s) associated to GO evidence codes. Annotating using the GO system is of importance for several reasons; the GO system captures defined concepts (the GO terms) with unique ids, which can be attached to specific genes and the three controlled vocabularies of the GO allow for the capture of much more annotation information than is traditionally captured in protein common names, including, for example, not just the function of the protein, but its location as well. GO evidence codes implemented in CharProtDB directly correlate with the GO consortium definitions of experimental codes. CharProtDB tools link characterization data from multiple input streams through synonymous accessions or direct sequence identity. CharProtDB can represent multiple characterizations of the same protein, with proper attribution and links to database sources. Users can use a variety of search terms including protein name, gene symbol, EC number, organism name, accessions or any text to search the database. Following the search, a display page lists all the proteins that match the search term. Click on the protein name to view more detailed annotated information for each protein. Additionally, each protein record can be annotated.
Proper citation: CharProtDB: Characterized Protein Database (RRID:SCR_005872) Copy
http://www.lasige.di.fc.ul.pt/webtools/proteinon/
ProteInOn calculates semantic similarity between GO terms or proteins annotated with GO terms. It also calculates term enrichment of protein sets, by applying a term representativity score, and gives additional information on protein interactions. The query compute protein semantic similarity returns the semantic similarity scores between all proteins entered, in matrix format. The option Measure allows users to choose one of several semantic similarity measures: Resnik, Lin, or Jiang & Conrath's measures with or without the DCA approach, plus the graph-based simUI and simGIC measures. These measures are listed by order of performance as evaluated with protein sequence similarity. The option GO type allows users to choose one of the aspects of GO: molecular function, biological process and cellular component. The option Ignore IEA limits the query to non-electronic annotations, excluding evidence types: IEA, NAS, ND, NR.
Proper citation: ProteInOn (RRID:SCR_005740) Copy
http://pbildb1.univ-lyon1.fr/virhostnet/
Public knowledge base specialized in the management and analysis of integrated virus-virus, virus-host and host-host interaction networks coupled to their functional annotations. It contains high quality and up-to-date information gathered and curated from public databases (VirusMint, Intact, HIV-1 database). It allows users to search by host gene, host/viral protein, gene ontology function, KEGG pathway, Interpro domain, and publication information. It also allows users to browse viral taxonomy.
Proper citation: VirHostNet: Virus-Host Network (RRID:SCR_005978) Copy
Web application to automate germline genomic variant curation from clinical sequencing based on ACMG guidelines. Aggregates multiple tracks of genomic, protein and disease specific information from public sources.
Proper citation: PathoMAN (RRID:SCR_026552) Copy
http://pridb.gdcb.iastate.edu/RPISeq
Web application for RNA-protein interactions prediction.
Proper citation: RPISeq (RRID:SCR_027257) Copy
https://www.tgh.org/institutes-and-services/cancer-institute/precision-medicine-bio-repository
Procures high-quality biologic specimens along with coded clinical and demographic data across broad ethnic, racial, and social demographic of patients. All specimens are systematically collected and processed so that their multi-functional potential for recovering high-quality bioanalytes (including RNA, genomic DNA, protein, enzymes and metabolites) is conserved. All specimens are stored and protected in a database hub to connect researchers conducting variety of scientific projects across multiple medical specialties. Muilti-disciplinary biorepository with capacity for generating specialized bioanalytes.
Proper citation: Tampa General Hospital-University of South Florida Health Precision Medicine Biorepository (RRID:SCR_027501) Copy
http://sites.northwestern.edu/htal/
Core provides expertise and resources for large scale biology. Helps to set up, run, gather data and perform analysis in drug discovery research, biochemistry, cell and organismal biology, functional genomic screening, and synthetic genetic. Works with proteins, nucleic acids, small model organisms, and microbial strains. Provides tissue culture,produces and uses lentivirus particles, screens compound libraries, does experiments for investigators,generates preliminary data to figure out if idea is workable, discusses project development. Services include Macromolecular binding, biochemical, and cell-based assays,High content screening with widefield or confocal optics,Nanoliter liquid handling up to 1536-well density,Whole-plate kinetic assays (ion currents, GPCR signaling),Compound library screening,CRISPR/Cas9 screening (multiplexed libraries),Analysis of large data sets,Fluorescence Thermal Shift assay (measures protein melting),Complex liquid handling work flows.
Proper citation: Northwestern University High Throughput Analysis Laboratory Core Facility (RRID:SCR_017879) Copy
Core mass spec and proteomic services include open access lab for trained users with GC/MS, LC/MS, high resolution LC/MS, and MALDI-TOF instruments, help with intact protein analysis, targeted quantitation, drug discovery support, pathway analysis, protein interactions, FFPE tissue analysis, both labeled and label-free proteomics, and more. Please contact SUMS to discuss these and other custom projects including new application development.
Proper citation: Stanford University Vincent Coates Foundation Mass Spectrometry Laboratory Core Facility (RRID:SCR_017801) Copy
http://rppc.mccormick.northwestern.edu/
Core provides quality controlled recombinant proteins. rPPC operates based on the two service models: Training model where Northwestern researchers use specialized bioreactor systems and participate in hands-on-training activities and Production model where staff carry out expression (mg to gm scale) and purification of recombinant or synthetic biologics, including potential therapeutic proteins and peptides, among others. Main focus of rPPC is to be user-facility;facility has parallel bioreactor systems for multiplexed lab-scale cultivation of microbial, insect, and mammalian cells. rPPC also serves as a production facility, providing low-cost recombinant biologics for researchers at Northwestern University.Services include: TRANSFECTION/TRANSFORMATION, ANALYTICAL (SMALL SCALE) EXPRESSION IN E.COLI AND MAMMALIAN CELLS,PROTEIN EXPRESSION IN E. COLI (LARGE SCALE),PROTEIN EXPRESSION IN MAMMALIAN CELL SYSTEM (LARGE SCALE),PROTEIN EXPRESSION IN INSECT CELL SYSTEM,GENERATION OF MOUSE HYBRIDOMA, PRODUCING MONOCLONAL ANTIBODIES, per one fusion,RESCUING AND CULTIVATING EUKARYOTIC CELLS,DOWNSTREAM PROCESSING OF GROWN CULTURE (BEFORE PROTEIN PURIFICATION),RECOMBINANT PROTEIN PURIFICATION,TAG CLEAVAGE WITH TEV. PROTEASE,LARGE SCALE mAb PRODUCTION ,DNA PLASMID PROPAGATION AND PURIFICATION,SDS-PAGE ANALYSIS,WESTERN BLOT ANALYSIS, INSTRUMENT TIME SHARING TECHNICAL/INSTRUMENT ASSISTANCE TIME,PROTEIN RECOVERING FROM INCLUSION BODIES.
Proper citation: Northwestern University Recombinant Protein Production Core Facility (RRID:SCR_017872) Copy
http://www.med.unc.edu/csb/pep
Core specializes in production of pure, functional proteins for structural, biophysical, and biochemical studies. Facility offers three categories of service:Protein Expression,Protein Purification,Scientific Consultation, Mentoring, and Training; Offers Isotope labeled proteins for NMR;High production scales for immunizations, drug discovery, structural biology;Endotoxin-free protein production;Stable cell line generation;Expert baculovirus expression;Custom packages to efficiently suit your needs.
Proper citation: North Carolina University at Chapel Hill School of Medicine Protein Expression and Purification Core Facility (RRID:SCR_017843) Copy
https://my.ilabsolutions.com/service_center/show_external/4003
Core specializes in cell, protein, and small molecules analysis as well as cell culture techniques. Services include:2-D gel electrophoresis, 2-D DIGE, LC-MS/MS, HPLC, flow cytometry, fluorescence-activated cell sorting (FACS), cell and tissue culture, and immortalization of cell lines. Our staff works closely with investigators to help design, perform, and analyze experiments.Offers training and assistance in flow cytometry, tissue culture, and operation many of our walk-up instruments.Instruments:Cell Sorter: FACS Aria III, BD Biosciences;Flow Cytometers, analyzers:C6, Accuri/BD Biosciences;Novocyte 3000, ACEA Biosciences;software for analysis: FSC Express, DeNovo software;LC-MS/MS: 6460 Triple Quadrupole, Agilent;Typhoon Trio Scanner, GE Lifesciences;Blood Analyzer: Hemavet 950, Drew Scientific.Plate Readers:;Victor Nivo 5F, Perkin Elmer;Luminometer: Centro XS, Berthold.Services:Cell Sorting (FACS);2-D gel electrophoresis/2D-DIGE;LC-MS/MS analysis of compounds; Cell immortilization.
Proper citation: Nemours/A.I.duPont Hospital for Children Cell Science Core Facility (RRID:SCR_017854) Copy
Core provides seven mass spectrometry platforms, for shotgun and targeted analyses, run by core staff. Services include protein and peptide identification from gels and solutions, identification and localization of post translational modifications, relative and absolute quantitation of peptides and proteins, intact mass analysis of proteins in solution.
Proper citation: UTSW Proteomics Core (RRID:SCR_017813) Copy
https://redoxbiologycenter.unl.edu/facilities/metabolomics-and-proteomics-core-facility/
Provides tools of modern functional proteomics and metabolomics. Facility is equipped with chromatography and mass spectrometry based technologies for proteomics and metabolomics (Clinical and non clinical), personalized experimental design consultation and comprehensive, individualized bioinformatics support.Services include:Small molecule exact mass determination or quantitation using positive or negative ion mode;Protein identification using LC/MS/MS analysis and MASCOT and SEQUEST database search;Shot gun proteome analysis of biological samples;Biomarker discovery from biological fluid;Drug protein or drug nucleic acid protein interaction;Protein complex isolation and identifying interacting partners and its quantitation;Protein differential expression analysis and quantitation by 2D-LC MS/MS (MudPIT);Global PTM analysis and quantitation;Specialization in phosphorylation and oxidation analysis;Coomassie Blue and Silver Stained Gel analysis; de novo peptide sequencing by tandem mass spectrometry;Confirmation of mutations in protein ;Customized sequence search of in-house proteins that are not available in database; Post translational modifications (phosphorylation, sumoylation, ubiquitination, oxidation, etc.); Determination of oxidation state of cysteine (disulfide bonds);Intact proteins and peptides mass determination.
Proper citation: Nebraska-Lincoln University Metabolomics and Proteomics Core Facility (RRID:SCR_017789) Copy
Core provides fully automated high throughput screening (HTS) of Compound Libraries (130,000+ compounds) for both enzyme/protein-based assays and cell-based assays, using Caliper Life Sciences Staccato system;Genomic siRNA screening with siARRAY whole human genome siRNA library from Dharmacon targeting 21,000 genes, using Agilent Bravo system;High-Content Screening using ImageXpress Micro automated fluorescent microscope with live cell, bright field, phase contrast and integrated plate handling with Thermo Catalyst CRS, and image analysis using MetaXpress software;High Throughput Molecular Biology reagents and services, including access to cDNA libraries (Human ORFeome collection, 15,000 genes) and 96 and 384-well bead clean-ups and PCR setup (Biomek FX and Agilent Bravo), and other automation steps in collaboration with SFGF;High-throughput assay development assistance with cell culture, experiment design, robotic programming and Standard Operating Procedure drafting;Screening data analysis assistance with protocols, hit determination and structure activity analyses using MDL chemical database ISIS/HOST, Plate Manager, Assay Explorer and Report Manager. Use of microplate reader detection systems, including Tecan Infinite M1000 and Infinite M1000 PRO and Molecular Devices Analyst GT for fluorescence; fluorescence polarization; time-resolved fluorescence; absorbance and luminescence (with injectors and AlphaScreen); and Flexstation II 384, for kinetic fluorescence reads to measure calcium mobilization and ion channels.Use of liquid-handling robots, including Sciclone ALH3000 (96- and 384-well pipetting), Agilent Bravo (96- and 384-well pipetting), Velocity11 VPrep (96-well pipetting), Bio-Tek plate washers/dispensers, Matrix Wellmate and Titertek/Labsystems Multidrop microplate dispensers, and Velocity11 PlateLoc plate heat sealer;Training for most of these services.
Proper citation: Stanford University School of Medicine High Throughput Bioscience Center Core Facility (RRID:SCR_017794) Copy
https://med.psu.edu/core/mass-spectrometry
Core provides mass spectrometry analyses and identification of proteins, peptides, oligonucleotides, carbohydrates and small molecules.Other services include separations of complex protein and/or peptide mixtures; protein expression analysis (iTraq, SILAC, SWATH/DIA label-free); quantitation of protein, cytokine, amino acid and other small-molecule levels; bioinformatics; spot-cutting and robotics; and gel imaging and analysis., THIS RESOURCE IS NO LONGER IN SERVICE. Documented on September 16,2025.
Proper citation: Penn State College of Medicine Mass Spectrometry and Proteomics Core Facility (RRID:SCR_017831) Copy
https://med.nyu.edu/research/scientific-cores-shared-resources/proteomics-laboratory
Core offers specialized expertise for analysis of proteins and peptides using mass spectrometry. Develops new methods and customized approaches for proteomic analysis and suggests experimental strategies and sample preparation prior to mass spectrometry analysis. Services include:comprehensive protein identification ,analysis of affinity purified complexes,characterizing protein post-translational modifications,de novo sequencing,label and label-free quantitation ,multiplexed quantitation global phosphorylation and ubiquitin analysis,analysis of laser-capture microdissected formalin-fixed paraffin-embedded tissue,secretome analysis,crosslinking analysis,disulfide mapping.
Proper citation: New York University School of Medicine Langone Health Proteomics Laboratory Core Facility (RRID:SCR_017926) Copy
Core provides liquid chromatography and gas chromatography mass spectrometry instrumentation for selective identification and reproducible quantification of trace-level biomolecules in complex samples. Services include qualitative, quantitative and structural analysis of proteins, lipids, metabolites, pesticides, pharmaceuticals and volatile organic compounds. Tests can be performed as long as molecules of interest are amenable to ionisation technique employed in source of mass spectrometer. Depending on instrument type, samples may be solid, liquid or gas. Mass spectrometry platforms include Liquid Chromatography Mass Spectrometry (LC-MS) and Gas Chromatography Mass Spectrometry (GC-MS). Analysis include volatile organic compounds (odour analysis),pharmacokinetics (bioavailability, bioefficacy),drug development (determining structures of drugs and metabolites),clinical testing (biomarkers discovery and endogenous compounds),genomics (oligonucleotide sequencing) epigenetics (global DNA methylation analysis),environmental research (testing water, soil, food and air quality).
Proper citation: Queensland University of Technology Central Analytical Research Facility (CARF) Proteomics and Small Molecule Mass Spectrometry Core Facility (RRID:SCR_017933) Copy
Core provides computational resources and expertise to enhance productivity of researchers studying infectious diseases. Assists with virtual screening, protein-small molecule docking, binding site prediction, protein modeling and design, prediction of protein stability changes upon mutation, fragment based probe design, as well as preparation of presentation graphics.Specializes in initial hit identification of non-traditional drug targets such as protein-protein or protein-RNA interfaces by offering high-throughput virtual screening via pocket optimization with exemplar screening at protein-protein interfaces and hotspot pharmacophore mimicry of protein-RNA interactions.CCB works in collaboration with Molecular Graphics and Modeling Laboratory.
Proper citation: Kansas University at Lawrence Computational Chemical Biology Core Facility (RRID:SCR_017890) Copy
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